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5MSQ

Structure of the A domain of carboxylic acid reductase (CAR) from Nocardia iowensis in complex with AMP and iodide

Functional Information from GO Data
ChainGOidnamespacecontents
A0001676biological_processlong-chain fatty acid metabolic process
A0004467molecular_functionlong-chain fatty acid-CoA ligase activity
A0005524molecular_functionATP binding
A0006629biological_processlipid metabolic process
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0031177molecular_functionphosphopantetheine binding
A0047683molecular_functionaryl-aldehyde dehydrogenase (NADP+) activity
A0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues19
Detailsbinding site for residue AMP A 1201
ChainResidue
AHIS300
ATHR421
AASP495
ATYR507
AARG510
ALYS616
AHOH1345
AHOH1376
AHOH1399
AHOH1435
AHOH1742
ASER395
AALA396
APRO397
AASP416
AGLY417
ATYR418
AGLY419
ASER420

site_idAC2
Number of Residues2
Detailsbinding site for residue IOD A 1202
ChainResidue
ASER299
AHOH1926

site_idAC3
Number of Residues2
Detailsbinding site for residue IOD A 1203
ChainResidue
AASN279
ASER280

site_idAC4
Number of Residues2
Detailsbinding site for residue IOD A 1204
ChainResidue
ALEU68
AHIS195

site_idAC5
Number of Residues1
Detailsbinding site for residue IOD A 1205
ChainResidue
AGLU479

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. SavrvvresyAngYGNSKWAGeVLLrEAH
ChainResidueDetails
ASER943-HIS971

site_idPS00455
Number of Residues12
DetailsAMP_BINDING Putative AMP-binding domain signature. LIYTSGSTGtPK
ChainResidueDetails
ALEU252-LYS263

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02247, ECO:0000269|PubMed:28719588, ECO:0007744|PDB:5MSC, ECO:0007744|PDB:5MSD, ECO:0007744|PDB:5MSQ
ChainResidueDetails
AHIS300
ASER395
AASP416
AASP495
ATYR507

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02247, ECO:0000269|PubMed:28719588, ECO:0007744|PDB:5MSD, ECO:0007744|PDB:5MSQ
ChainResidueDetails
ATHR421
ALYS616

site_idSWS_FT_FI3
Number of Residues9
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02247
ChainResidueDetails
ALYS516
AASN787
AARG814
AARG824
APRO880
ASER920
ATYR956
ALYS960
ASER983

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: O-(pantetheine 4'-phosphoryl)serine => ECO:0000255|HAMAP-Rule:MF_02247, ECO:0000269|PubMed:17102130
ChainResidueDetails
ASER689

226707

PDB entries from 2024-10-30

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